Journal
BIOCHEMISTRY
Volume 50, Issue 12, Pages 1966-1980Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi101885m
Keywords
-
Categories
Funding
- National Institutes of Health [HG004508-03, CA87658-10, CA80058-11, DA028776-01]
- New York State Department of Health NYSTEM [N08G-498]
Ask authors/readers for more resources
Histone methylation recognition is accomplished by a number of evolutionarily conserved protein domains, including those belonging to the methylated lysine-binding Royal family of structural folds. One well-known member of the Royal family, the chromodomain, is found in the HP1/chromobox and CHD subfamilies of proteins, in addition to a small number of other proteins that are involved in chromatin remodeling and gene transcriptional silencing. Here we discuss the structure and function of the chromodomain within these proteins as methylated histone lysine binders and how the functions of these chromodomains can be modulated by additional, post-translational modifications or binding to nucleic acids.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available